Related Experiment Video
Updated: Jun 25, 2026

Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding
Published on: September 21, 2011
Glucocorticoid receptor (GR) beta has intrinsic, GRalpha-independent transcriptional activity
Tomoshige Kino1, Irini Manoli, Sujata Kelkar
1Program in Reproductive and Adult Endocrinology, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892-1109, USA. kinot@mail.nih.gov
Abstract:
The human glucocorticoid receptor (GR) gene produces C-terminal GRbeta and GRalpha isoforms through alternative use of specific exons 9beta and alpha, respectively. We explored the transcriptional activity of GRbeta on endogenous genes by developing HeLa cells stably expressing EGFP-GRbeta or EGFP. Microarray analyses revealed that GRbeta had intrinsic gene-specific transcriptional activity, regulating mRNA expression of a large number of genes negatively or positively. Majority of GRbeta-responsive genes was distinct from those modulated by GRalpha, while GRbeta and GRalpha mutually modulated each other's transcriptional activity in a subpopulation of genes. We did not observe in HCT116 cells nuclear translocation of GRbeta and activation of this receptor by RU 486, a synthetic steroid previously reported to bind GRbeta and to induce nuclear translocation. Our results indicate that GRbeta has intrinsic, GRalpha-independent, gene-specific transcriptional activity, in addition to its previously reported dominant negative effect on GRalpha-induced transactivation of GRE-driven promoters.
More Related Videos
Related Concept Videos
TGF - β Signaling Pathway
Co-activators and Co-repressors
Transducer Mechanism: Nuclear Receptors
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:
General Transcription Factors
Master Transcription Regulators
Master Transcription Regulators

